Interaction of aconitine with bovine serum albumin and effect of atropine sulphate and glycyrrhizic acid on the binding |
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Authors: | Yun Huang Li-Jian Cui Jian-Ming Wang Kun Huo Chen Chen Wen-Hong Zhan Yong-Li Wang |
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Institution: | 1. Pharmaceutical College, Hebei Medical University, 361 Zhongshan East Road, Shijiazhuang City, Hebei Province 050017, People''s Republic of China;2. Traditional Chinese Medical College, Hebei Medical University, Shijiazhuang 050091, People''s Republic of China |
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Abstract: | The interaction of aconitine with bovine serum albumin (BSA) and effect of atropine sulphate and glycyrrhizic acid on binding constant, binding sites, and conformation were studied in an aqueous buffer solution (pH 7.40) by ultraviolet absorption and fluorescence spectroscopy. The study results show that aconitine quenched the endogenous fluorescence of BSA via a dynamic quenching procedure. Predominant intermolecular forces between aconitine and BSA were hydrophobic interactions, which stabilized the complex of aconitine–BSA. The distance between the donor and acceptor was 2.62 nm. The conformation of BSA was investigated by synchronous fluorescence techniques, indicating that the microenvironment around tryptophan (Trp) residues was changed. Furthermore, with the addition of atropine sulphate or glycyrrhizic acid, binding constant and the number of binding sites of aconitine to BSA were decreased, and the conformation had no change, which provide an important theoretical support for aconitine detoxification by atropine sulphate and glycyrrhizic acid. |
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